Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line.
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β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptidesEarly mechanisms of pathobiology are revealed by transcriptional temporal dynamics in hippocampal CA1 neurons of prion infected miceCell line specific modulation of extracellular aβ42 by Hsp40Mutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC α(2)δ-1 SubunitEfficacy of novel acridine derivatives in the inhibition of hPrP90-231 prion protein fragment toxicity.Epidemiological mechanisms of genetic resistance to kuru.Human PrP90-231-induced cell death is associated with intracellular accumulation of insoluble and protease-resistant macroaggregates and lysosomal dysfunction.Structural diversity and initial oligomerization of PrP106-126 studied by replica-exchange and conventional molecular dynamics simulationsMembrane-mediated amyloid formation of PrP 106-126: A kinetic study.The Effects of Ca2+ Concentration and E200K Mutation on the Aggregation Propensity of PrPC: A Computational Study.Mapping the parameters of prion-induced neuropathology.Possible role for Ca2+ in the pathophysiology of the prion protein?Prion protein and its role in signal transduction.The changing landscape of voltage-gated calcium channels in neurovascular disorders and in neurodegenerative diseasesDifferent Molecular Mechanisms Mediate Direct or Glia-Dependent Prion Protein Fragment 90-231 Neurotoxic Effects in Cerebellar Granule Neurons.Membrane Disruption Mechanism of a Prion Peptide (106-126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy.Using protein misfolding cyclic amplification generates a highly neurotoxic PrP dimer causing neurodegeneration.Sphingosine kinase-dependent migration of immature dendritic cells in response to neurotoxic prion protein fragment.The mechanism of membrane disruption by cytotoxic amyloid oligomers formed by prion protein(106-126) is dependent on bilayer composition.Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231.Neurotrophin p75 receptor is involved in neuronal damage by prion peptide-(106-126).PrP(106-126) does not interact with membranes under physiological conditions.Prion peptide induces neuronal cell death through a pathway involving glycogen synthase kinase 3Channel activity of deamidated isoforms of prion protein fragment 106-126 in planar lipid bilayers.Prion protein fragment 106-126 potentiates catecholamine secretion from PC-12 cells.Involvement of calcineurin in the neurotoxic effects induced by amyloid-beta and prion peptides.Amidation and structure relaxation abolish the neurotoxicity of the prion peptide PrP106-126 in vivo and in vitro.Neurotoxicity of prion peptide 106-126 not confirmed.Excitotoxicity through NMDA receptors mediates cerebellar granule neuron apoptosis induced by prion protein 90-231 fragment.A nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons.Methionine oxidation of amyloid peptides by peroxovanadium complexes: inhibition of fibril formation through a distinct mechanism.Prion peptide fragment PrP[106-126] forms distinct cation channel types.
P2860
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P2860
Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Prion protein fragment 106-126 ...... activity in the GH3 cell line.
@en
type
label
Prion protein fragment 106-126 ...... activity in the GH3 cell line.
@en
prefLabel
Prion protein fragment 106-126 ...... activity in the GH3 cell line.
@en
P2093
P2860
P1476
Prion protein fragment 106-126 ...... activity in the GH3 cell line.
@en
P2093
F Tagliavini
G Schettini
S Thellung
P2860
P304
P356
10.1002/(SICI)1097-4547(19981101)54:3<341::AID-JNR5>3.0.CO;2-G
P577
1998-11-01T00:00:00Z